“…For example, upon comparison of the electrochemical data obtained for α-helical peptides, it is evident that the rate constants of electron transfer vary significantly although the lengths of the spacers are similar. , This probably reflects the differences in the details of amino acid sequences. Several groups have also demonstrated the influence of the secondary structure of the peptide on electron-transfer efficiency. − Shin and co-workers showed in their theoretical study that the parameter that describes the ability of the bridge to mediate the electron transfer, i.e., the distance decay constant (β), is sensitive to the secondary structure of the peptide backbone in the case of the superexchange mechanism . Ghiggino and co-workers observed the different distance dependences for photoinduced electron transfer through α-helical and β-sheet structures and found corresponding decay constants of 0.66 and 0.73 Å -1 , respectively. , A very weak distance dependence for 3 10 -helices of aminoisobutyric oligomers was reported by Maran and co-workers, who attributed this result to the effect of intramolecular hydrogen bonding on the electron-transfer rate .…”